RESEARCH NOTE THE EFFECTS OF SALTS ON THERMAL TRANSITION CURVES OF COD MUSCLE

Examination of the thermograms of cod muscle to which various salts have been added indicate that NaI decreases transition energies of both myosin and actin as compared to a no salt control, and to NaCl and Na₂SO₄ treated samples. In contrast, CaCl₂ and MgCl₂ increases but broadens the peaks.     

Formulation Protocol and Dicationic Salts Affect Protein Functionality of Model System Beef Batters

ABSTRACT: The objective of this study was to determine if addition, and order of addition, of CaCl₂ and MgCl₂ affected protein functionality of lean beef preblends. Four treatments were applied to non-preblended (NPB) batters prior to thermal processing. Six treatments were applied to preblended (PB) batters 12 h prior to thermal processing. All treatments contained 2% NaCl. Dicationic salts decreased raw pH in NPB and PB batters, while cooked pH was unaffected. Magnesium chloride in NPB and CaCl₂+ MgCl₂ in PB batters resulted in the highest total soluble protein (TSP). Calcium chloride + MgCl₂ in NPB batters resulted in firmer gels compared to the control. Magnesium chloride, in both NPB and PB, caused the greatest increase in soluble myosin, and preblending decreased myosin solubility.     

THE EFFECT OF pH, POLYPHOSPHATES AND DIFFERENT SALTS ON WATER RETENTION PROPERTIES OF GROUND TROUT MUSCLE

The water binding potential (WBP) and expressible moisture (EM) curves of ground rainbow trout white muscle versus pH are different, particularly in the region from pH 5.0 to 7.0. The effect of different salts such as CaCl₂, Mg Cl₂, NaCl, Nal and Na₂SO₄ on WBP suggests that for the same salts, cations cause a smaller change than anions. On the other hand, the EM measurements suggest that cations have a greater effect on this measurement than anions. In the case of WBP, the effect of tripolyphosphate and pyrophosphate can be attributed solely to their effect on pH. These results indicate the differences between the two methods and suggest that they measure different components of the water retention properties of a complex system, and thus water holding capacity measurements must be interpreted with care.     

Fractionating Soybean Storage Proteins Using Ca2+ and NaHSO3

ABSTRACT:  Individual soybean storage proteins have been identified as having nutraceutical properties, especially β-conglycinin. Several methods to fractionate soy proteins on industrial scales have been published, but there are no commercial products of fractionated soy proteins. The present study addresses this problem by using calcium salts to achieve glycinin-rich and β-conglycinin-rich fractions in high yields and purities. A well-known 3-step fractionation procedure that uses SO_2, NaCl, and pH adjustments was evaluated with CaCl₂ as a substitute for NaCl. Calcium was effective in precipitating residual glycinin, after precipitating a glycinin-rich fraction, into an intermediate fraction at 5 to 10 mM CaCl₂ and pH 6.4, eliminating the contaminant glycinin from the β-conglycinin-rich fraction. Purities of 100%β-conglycinin with unique subunit compositions were obtained after prior precipitation of the glycinin-rich and intermediate fractions. The use of 5 mM SO₂ in combination with 5 mM CaCl₂ in a 2-step fractionation procedure produced the highest purities in the glycinin-rich (85.2%) and β-conglycinin-rich (80.9%) fractions. The glycinin in the glycinin-rich fraction had a unique acidic (62.6%) to basic (37.4%) subunit distribution. The β-conglycinin-rich fraction was approximately evenly distributed among the β-conglycinin subunits (30.9%, 35.8%, and 33.3%, for α', α, and β subunits, respectively). Solids yields and protein yields, as well as purities and subunit compositions, were highly affected by pH and SO₂ and CaCl₂ concentrations.     

Viscoelasticity of Frozen/Thawed Egg Yolk as Affected by Salts, Sucrose and Glycerol

Based on dynamic rheological measurements, sucrose, glycerol and magnesium chloride (MgCl₂) prevented egg yolk gelation at concentrations of 2% and higher. These additives showed improved cryoprotectant effects as their concentrations were increased. Sodium chloride (NaCl) at higher than 2% also prevented gelation but at 10%, it caused a considerable increase in viscosity of unfrozen yolk. Calcium chloride (CaCl₂) showed an opposite effect, promoting protein coagulation before freezing. Samples with 2% CaCl₂ gelled completely after 36h at -24°C. Before freezing, potassium chloride (KCl) in the range 2–10% had an effect similar to that of NaCl. However, after freezing its effect changed. Yolk with 2% KCl, frozen 36h at -24°C, showed very elastic behavior.     

Effect of the addition of trisodium citrate and calcium chloride during salting on the rheological and textural properties of Cheddar-style cheese during ripening

The effect of addition of trisodium citrate (TSC) and calcium chloride (CaCl₂) on the textural and rheological properties of Cheddar-style cheese was investigated. Cheese curds were salted (2.5%) with NaCl (control) or NaCl supplemented with either TSC or CaCl₂ with a constant ionic strength. Casein-bound calcium phosphate decreased upon addition of TSC and increased upon addition of CaCl₂. Addition of CaCl₂ resulted in increased hardness. Addition of TSC resulted in reduced hardness but more elastic cheeses at high temperatures. The addition of TSC or CaCl₂ at salting had a significant effect on cheese rheology and texture.     

Formation of Soy Protein Isolate Cold-set Gels: Protein and Salt Effects

ABSTRACT: The influence of protein and calcium concentration on soy protein cold-set gel formation and rheology has been investigated. Cold-set gels can be formed at soy protein concentrations from 6% to 9% and calcium concentrations from 10 to 20 mM. Gel properties can be modulated by changing the protein and/or CaCl₂ concentrations. An increase in CaCl₂ concentration from 10 to 20 mM increased gel opacity while an increase in protein concentration from 6% to 9% decreased opacity. Water-holding capacity improved with increasing protein concentration and decreasing CaCl₂ concentration. The elastic modulus (G') increased with protein and calcium chloride concentrations. Microscopy revealed an increase in the diameters of aggregates and pores as CaCl₂ concentration increased and as protein concentration decreased. Cold-set gels with a broad range of characteristics can be obtained from soy protein.     

Isolation of Tomato Seed Meal Proteins with Salt Solutions

Salt solutions were used in isolating tomato seed meal proteins. Na₂SO₃ and NaCl solutions at different concentrations, and pH were included in a central composite design to find optimum conditions of protein isolation. The highest total protein yield was achieved with water extraction (no salt present). Salt extraction at pH 7.5 produced isolates with protein content of 93.4% (NaCl 5% w/v) and 77.1% (Na₂SO₃ 0.5% w/v). Observed values were in good agreement with predicted values. Isolates extracted with different salt solutions ranged from less soluble but very resistant to heat and Ca²⁺, to very surface active with functional properties comparable to commercial soy isolates.     

MEASURING THE WATER HOLDING CAPACITY OF NATURAL ACTOMYOSIN FROM CHICKEN BREAST MUSCLE IN THE PRESENCE OF PYROPHOSPHATE AND DIVALENT CATIONS

The water holding capacity (WHC) of natural actomyosin (NAM) extracted at pH 9.2 in 0.6M KCl was measured in the presence and absence of various combination of sodium pyrophosphate (PP_i), MgCl₂ and CaCl₂ using a modification of the classical centrifugation technique. Samples, in the presence of 0.15M NaCl and 20 mM sodium phosphate buffer pH 6, were spun at 30,900 X G (as measured at the bottom of the centrifuge tube) for 15 min at 2–4C. The results show that between 17 and 20 g water/g protein were bound over a wide range of NAM concentrations. In each case the amount of water held by the experimental sample was equal to or less than the amount held by a control run at the same time: 5 mM PP_i= 100%; 5 mM PP_i+ 5 mM MgCl₂= 58%; 5 mM MgCl₂= 85%; 5 mM PP_i+ 5 mM CaCl₂= 68% and 5 mM CaCl₂= 92% of the control. Thus polyphosphate addition in the presence of divalent cations lowers the WHC of NAM. The absence of the organized structure of muscle in NAM is postulated to be the reason that polyphosphate plus divalent cation reduced WHC in these samples. A series of preliminary experiments were run in order to determine the effect of experimental parameters on WHC.     

EFFECT OF ELECTRICAL STIMULATION ON KILLING SALMONELLA TYPHIMURIUM IN VARIOUS SALT SOLUTIONS

Electrical stimulation was evaluated as a method to kill Salmonella typhimurium in various salt solutions at different concentration . Salmonella typhimurium at 2 × 10⁵ CFU/ml was treated at 22–24C for 60 min in each salt solution using electricity at 10 mA/cm² current, 1 kHz frequency, and 50% duty cycle. Samples taken at various times were serially diluted, plated on tryptic soy agar and xylose lysine desoxycholate agar, and incubated at 37C for 18–24 h. To detect injured cells, samples were also pre-enriched in buffered peptone water at 37C for 4–5h before being plated. Results indicated all salmonellae were electrically killed at 5 min in NaCl, at 30 min in NaNO₃, and at 45 min in NaC₂H₃O₂ at 0.15 and 0.015 M concentrations. Salmonellae were also killed at 45 min in Na₃PO₄ and at 60 min in Na₂CO₃ at 0.0015 M concentration by electricity in combination with high pH .     

Factors Determining Yield Stress and Overrun of Whey Protein Foams

ABSTRACT: Foams were formed by whipping whey protein solutions (15% w/v protein) containing NaCl, CaCl₂, lactose, or glycine. Foam overrun and yield stress were determined. Foams made from whey protein ingredients have greater overrun and yield stress if the concentration of β-lactoglobulin is high relative to a-lactalbumin. The presence of 0.4 M CaCl₂ in the foaming solution increases overrun and yield stress for β-lactoglobulin and a-lactalbumin. The high yield stress of β-lactoglobulin and a-lactalbumin foams made from solutions containing CaCl₂ suggests that CaCl₂ is altering rheological properties of the interfacial protein film and/or contributing to protein aggregation or network formation in the lamellae.     

Calcium Chloride Added to Irrigation Water of Mushrooms (Agaricus Bisporus) Reduces Postharvest Browning

The influence of 0.3% CaCl₂ added to irrigation water on mushroom tyrosinase activity and postharvest browning was examined. Calcium concentration of mushrooms was significantly increased with the addition CaCl₂ to irrigation water but had no effect on inherent tyrosinase activity but reduced postharvest browning. The CaCl₂ had even more pronounced improvement in shelf life as indicated by reduced browning following a standard bruising treatment. Transmission electron micrographs indicate that increased levels of calcium in mushrooms irrigated with CaCl₂may have decreased browning by increasing vacuolar membrane integrity; thereby reducing the opportunity for tyrosinase to react with its substrates.     

Characterisation of soybean glycinin and β-conglycinin fractionated by using MgCl2 instead of CaCl2

A simple two step precipitation method was used to investigate the effect of MgCl₂ instead of CaCl₂ on fractionation of soybean glycinin and β-conglycinin. Compositional and physicochemical properties of the resulting protein fractions were characterised. The optimised procedure, in terms of protein yield, purity, phytate content and physicochemical properties, was obtained when the addition of 5 m m MgCl₂ was used. After application of 5 m m MgCl₂, the phytate content of the glycinin-rich and β-conglycinin-rich fractions was about 0.4% and 1.3%, respectively, but the addition of 5 m m CaCl₂ increased the phytate content of the glycinin-rich fraction to 1.25% and decreased that of β-conglycinin-rich fraction to 0.67%. Low phytate protein product was suitable for use in infant formula and acidic food. The solubility of the glycinin-rich fractions with MgCl₂ was significantly higher than that with CaCl₂ at pH < 4.5. Application of MgCl₂ improved thermal stability of the β-conglycinin-rich fraction.     

Incorporation of Soymilk Lipid into Soy Protein Coagulum by the Addition of Calcium Chloride

ABSTRACT: The effect of protein composition on the lipid incorporation into protein coagulum (tofu curd) was investigated using soymilk prepared from mixtures of glycinin-rich and β-conglycinin-rich soybeans. The lipid incorporation takes place with the addition of CaCl₂ so that a particulate fraction of the protein is aggregated. The incorporation occurred by less addition of CaCl₂ with increasing glycinin in soymilk. The protein particle content and the glycinin content of the particles increased along with increasing glycinin. The lipid incorporation took place at lower CaCl₂ concentration when the particulate glycinin content was high. The mechanism of the lipid incorporation into soybean curd is discussed from these results.     

Factors that affect the aggregation of rennet-altered casein micelles at low temperatures

The effects of temperature, CaCl₂ concentration, pH and ionic strength of milk on the aggregation of casein micelles in milk renneted at 15ºC were studied using particle size analysis determined by laser-light scattering. The rate of aggregation of rennet-altered casein micelles became significantly slower on reducing the temperature of renneting from 30 to 10ºC. At 15ºC, the rate of aggregation of rennet-altered casein micelles increased significantly on adding CaCl₂, on reducing the pH of renneted milk or on adding NaCl (up to 50 m m ). These results indicate that particle size analysis can be used successfully to study the aggregation of rennet-altered casein micelles.     

Proteolysis levels of white cheeses salted and ripened in brines prepared from various salts

This study was carried out to investigate the effects of salting and ripening periods in brines, prepared from various salts, on the properties of white cheeses. The brines were made from a mixture of NaCl with CaCl₂, KCl and MgCl₂ at 1 : 1 (molar basis) ratio. The NaCl solution alone was used as a control. The effects of different brines on total nitrogen, water-soluble nitrogen, nonprotein nitrogen, casein nitrogen and proteose-peptone nitrogen contents of cheeses were found to be insignificant, whereas the effect of ripening period on these properties was found to be significant ( P  < 0.05).     

EFFECT OF SEVERAL VARIABLES ON THE EXTRACTABILITY OF SUNFLOWER SEED PROTEINS

SUMMARY— The effect of several variables on the extraction of sunflower seed protein has been investigated. Solubility studies on the meal show that globulin is the main protein component. Albumin, nonprotein nitrogen and insoluble nitrogen are very low. Glutelin comprises about 17% of the total nitrogen. 15 min and a meal to solvent ratio of 1:10 (w/v) were found to extract a maximum amount of protein at pH 7.0. The optimum temperature of extraction is 45°C, although over a temperature range of 26-6°C the extraction remains essentially constant. More protein was extracted by 1.0 M NaCl and 0.75 M CaCl₂ at various pH's than by the higher or the lower concentrations of these salts. Results with several other salts show that concentration as well as pH is very important. Reducing agents do not appear to have any marked effect on the extractability of protein.     

Optimization of Medium Composition for Cultivating Clostridium butyricum with Response Surface Methodology

ABSTRACT: Probiotic bacteria, such as some strains of Clostridium butyricum , have been frequently used as the active ingredient in functional foods. However, slow growth of the probiotic bacteria has been one of the big concerns for their potential commercial application. In the present study, a fractional factorial design was applied to investigate the main factors, namely, the concentrations of the glucose, tryptone, yeast extract, beef extract, cys-teine, (NH₄) ₂SO₄, NaCl, K₂HPO₄, and the medium initial pH that affected the growth of 1 probiotic strain, C. butyricum ZJUCB, currently preserved in our laboratory. Central composite experimental design and response surface methodology were adopted to derive a statistical model for optimizing the composition of the medium. The experimental results showed that the optimum medium for incubating the C. butyricum ZJUCB was composed of 2.44% (w/v) glucose, 2.08% yeast extract (w/v), 1% tryptone (w/v), 0.1% (NH₄)₂SO₄ (w/v), 0.1% NaHCO₃ (w/v), 0.02% MnSO₄. H₂O (w/v), 0.02% MgSO₄. 7H₂O (w/v), 0.002% CaCl₂ (w/v), and 2% agar (w/v) (if necessary) at pH 8.55. After incubation for 24 h in the optimum medium, the populations of the viable organisms could reach 10⁹ colony-forming units (CFU)/mL, which was 100 times higher than that incubated in the initial medium.     

UNIAXIAL COMPRESSION OF GELS MADE FROM PROTEIN AND K-CARRAGEENAN

Investigations of gels (18% total solids) made from pea protein isolates (PPI) or soy protein isolate (SPI) with differing amounts of _K-carrageenan added showed that the gel strength increased with the concentration of _K-carrageenan. When the concentration of_K-carrageenan exceeded 0.4%, gels made with PPI were stronger and more stiff than equivalent gels made with SPI. Addition of _K-carrageenan stabilized gels made with PPI towards variations in brittleness (indicated by strain at fracture) with pH. This was not the case when SPI was used. Preheating (75C, 2 min) suspensions containing protein isolates and _K-carrageenan before gel formation increased the strength and stiffness of the final gels, most pronounced when SPI was used. Addition of NaCl (0.5–2%) reduced strength and stiffness of gels, whereas CaCl₂ had no influence on gel properties. Mixtures of PPI and SPI proved to be weaker and more brittle than gels made from only SPI of PPI. Results indicate that using proteins of different origin can cause differences in gel structure.     

Rheological properties of commercial whey protein samples from the MADGELAS survey

Summary Thermally induced gelation of commercial whey protein samples from the Molecular Basis of the Aggregation, Denaturation, Gelation and Surface Activity of Whey Proteins ( MADGELAS ) survey has been studied in order to develop a current status report on their rheological properties. Solutions of 10% protein (w/v) were prepared in distilled water, 200 mm NaCl or 10 mm CaCl₂ at neutral pH. Small-scale deformation of the samples was measured by dynamic oscillatory rheometry using a Bohlin CS Rheometer. Large-scale deformation at penetration mode was measured using a Texture Analyser (Stable Micro Systems, Surrey, UK). For solutions containing salts, there was a general trend for gel point to decrease and G' values to increase, the effect being more marked in the presence of NaCl. Similarly, force values at failure also tended to increase in the presence of salts. Results obtained with samples of similar protein composition dissolved in water were highly scattered, these differences being reduced in the presence of added salts.